Calpain-3 is autolyzed and hence activated in human skeletal muscle 24 h following a single bout of eccentric exercise

J Appl Physiol (1985). 2007 Sep;103(3):926-31. doi: 10.1152/japplphysiol.01422.2006. Epub 2007 Jun 21.

Abstract

The function and normal regulation of calpain-3, a muscle-specific Ca(2+)-dependent protease, is uncertain, although its absence leads to limb-girdle muscular dystrophy type 2A. This study examined the effect of eccentric exercise on calpain-3 autolytic activation, because such exercise is known to damage sarcomeric structures and to trigger adaptive changes that help prevent such damage on subsequent exercise. Six healthy human subjects performed a 30-min bout of one-legged, eccentric, knee extensor exercise. Torque measurements, vastus lateralis muscle biopsies, and venous blood samples were taken before and up to 7 days following the exercise. Peak isometric muscle torque was depressed immediately and at 3 h postexercise and recovered by 24 h, and serum creatine kinase concentration peaked at 24 h postexercise. The amount of autolyzed calpain-3 was unchanged immediately and 3 h after exercise, but increased markedly (from approximately 16% to approximately 35% of total) 24 h after the exercise, and returned to preexercise levels within 7 days. In contrast, the eccentric exercise produced little autolytic activation of the ubiquitous Ca(2+)-activated protease, mu-calpain. Eccentric exercise is the first physiological circumstance shown to result in calpain-3 activation in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adolescent
  • Adult
  • Calpain / metabolism*
  • Creatine Kinase / blood
  • Exercise / physiology*
  • Female
  • Humans
  • Male
  • Muscle Proteins / metabolism*
  • Quadriceps Muscle / metabolism*
  • Time Factors
  • Torque

Substances

  • Muscle Proteins
  • Creatine Kinase
  • CAPN3 protein, human
  • Calpain
  • mu-calpain